메뉴 건너뛰기




Volumn 18, Issue 2, 2004, Pages 323-330

Vibrational spectroscopy and computer modeling of proteins: Solving structure of α1-acid glycoprotein

Author keywords

Binding site; Fourier transform infrared spectroscopy; Molecular modeling; Orosomucoid; Raman spectroscopy; Thermal dynamics

Indexed keywords

BIOLOGICAL MEMBRANES; CARBOHYDRATES; MATHEMATICAL MODELS; MOLECULAR DYNAMICS; MOLECULAR VIBRATIONS;

EID: 2442668918     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.1155/2004/747828     Document Type: Conference Paper
Times cited : (11)

References (21)
  • 3
    • 0036805825 scopus 로고    scopus 로고
    • Study of chaperone-like activity of human haptoglobin: Conformational changes under heat shock conditions and localization of interaction sites
    • R. Ettrich, W. Brandt, V. Kopecký Jr., V. Baumruk, K. Hofbauerová and Z. Pavlíček, Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites, Biol. Chetn. 383 (2002), 1667-1676.
    • (2002) Biol. Chetn. , vol.383 , pp. 1667-1676
    • Ettrich, R.1    Brandt, W.2    Kopecký Jr., V.3    Baumruk, V.4    Hofbauerová, K.5    Pavlíček, Z.6
  • 5
    • 0002912034 scopus 로고
    • Preparation and properties of serum and plasma proteins XXIX
    • K. Schmid, Preparation and properties of serum and plasma proteins XXIX, J. Am. Chem. Soc. 75 (1953), 60-68.
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 60-68
    • Schmid, K.1
  • 9
    • 0024622619 scopus 로고
    • On the spectral subtraction of water from the FT-IR spectra of aqueous solutions of proteins
    • F. Dousseau, M. Therrien and M. Pézolet, On the spectral subtraction of water from the FT-IR spectra of aqueous solutions of proteins, Appl. Spectrosc. 43 (1989), 538-542.
    • (1989) Appl. Spectrosc. , vol.43 , pp. 538-542
    • Dousseau, F.1    Therrien, M.2    Pézolet, M.3
  • 10
    • 0027136282 scopus 로고
    • Comparative modelling by satisfaction of spatial restraints
    • A. Sali and T.L. Blundell, Comparative modelling by satisfaction of spatial restraints, J. Mol. Biol. 234 (1993), 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 11
    • 0032477320 scopus 로고    scopus 로고
    • Regulation of β-sheet structures within amyloid-like β-sheet assemblage from tripeptide derivatives
    • N. Yamada, K. Ariga, M. Naito, K. Matsubara and E. Koyama, Regulation of β-sheet structures within amyloid-like β-sheet assemblage from tripeptide derivatives, J. Am. Chem. Soc. 120 (1998), 12192-12199.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12192-12199
    • Yamada, N.1    Ariga, K.2    Naito, M.3    Matsubara, K.4    Koyama, E.5
  • 12
    • 0024997389 scopus 로고
    • Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods
    • F. Dousseau and M. Pézolet, Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods, Biochemistry 29 (1990), 8771-8779.
    • (1990) Biochemistry , vol.29 , pp. 8771-8779
    • Dousseau, F.1    Pézolet, M.2
  • 13
    • 0022503458 scopus 로고
    • Protein secondary structure analysis using Raman amide I and III spectra
    • R.W. Williams, Protein secondary structure analysis using Raman amide I and III spectra, Methods Enzymol. 130 (1986), 311-331.
    • (1986) Methods Enzymol. , vol.130 , pp. 311-331
    • Williams, R.W.1
  • 14
    • 33847797592 scopus 로고
    • Raman spectra of strained disulfides. Effect of rotation about sulfur-sulfur bonds on sulfur stretching frequencies
    • H.E. Van Wart and H.A. Scheraga, Raman spectra of strained disulfides. Effect of rotation about sulfur-sulfur bonds on sulfur stretching frequencies, J. Phys. Chem. 80 (1976), 1823-1832.
    • (1976) J. Phys. Chem. , vol.80 , pp. 1823-1832
    • Van Wart, H.E.1    Scheraga, H.A.2
  • 15
    • 0017263227 scopus 로고
    • 1-acid glycoprotein for characterization of the progesterone binding site
    • 1- acid glycoprotein for characterization of the progesterone binding site, Biochim. Biophys. Acta 168 (1976), 195-213.
    • (1976) Biochim. Biophys. Acta , vol.168 , pp. 195-213
    • Kute, T.1    Westphal, U.2
  • 17
    • 0028852391 scopus 로고
    • Heat denaturation of human orosomucoid in water-methanol mixtures
    • M. Kodíček, A. Infanzón and V. Karpenko, Heat denaturation of human orosomucoid in water-methanol mixtures, Biochim. Biophys. Acta 1246 (1995), 10-16.
    • (1995) Biochim. Biophys. Acta , vol.1246 , pp. 10-16
    • Kodíček, M.1    Infanzón, A.2    Karpenko, V.3
  • 21
    • 0041885136 scopus 로고    scopus 로고
    • +-ATPase N-domain at 2.6 Å resolution
    • +-ATPase N-domain at 2.6 Å resolution, J. Mol. Biol. 332 (2003), 1175-1182.
    • (2003) J. Mol. Biol. , vol.332 , pp. 1175-1182
    • Håkansson, K.O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.